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  2. Iron–sulfur protein - Wikipedia

    en.wikipedia.org/wiki/Ironsulfur_protein

    Iron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins , such as the ferredoxins , as well as NADH dehydrogenase , hydrogenases , coenzyme Q – cytochrome ...

  3. Iron–sulfur cluster - Wikipedia

    en.wikipedia.org/wiki/Ironsulfur_cluster

    Iron–sulfur clusters are molecular ensembles of iron and sulfide. They are most often discussed in the context of the biological role for iron–sulfur proteins , which are pervasive. [ 2 ] Many Fe–S clusters are known in the area of organometallic chemistry and as precursors to synthetic analogues of the biological clusters.

  4. Iron–sulfur cluster biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Ironsulfur_cluster...

    Finally these Fe-S cluster is transferred to a target protein, which then become functional. [1] The formation of iron–sulfur clusters are produced by one of four pathways: [2] Nitrogen fixation (NIF) system, which is also found in bacteria that are not nitrogen-fixing. [3] Iron–sulfur cluster (ISC) system, in bacterial and mitochondria

  5. Iron in biology - Wikipedia

    en.wikipedia.org/wiki/Iron_in_biology

    Iron is required for life. [1] [2] [3] The iron–sulfur clusters are pervasive and include nitrogenase, the enzymes responsible for biological nitrogen fixation.Iron-containing proteins participate in transport, storage and use of oxygen. [1]

  6. Rieske protein - Wikipedia

    en.wikipedia.org/wiki/Rieske_protein

    In 1979, Trumpower's team isolated the "oxidation factor" from bovine mitochondria and showed it was a reconstitutively-active form of the Rieske iron-sulfur protein. [2] It is a unique [2Fe-2S] cluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues.

  7. Cytochrome b6f complex - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_b6f_complex

    The cytochrome b 6 f complex is a dimer, with each monomer composed of eight subunits. [3] These consist of four large subunits: a 32 kDa cytochrome f with a c-type cytochrome, a 25 kDa cytochrome b 6 with a low- and high-potential heme group, a 19 kDa Rieske iron-sulfur protein containing a [2Fe-2S] cluster, and a 17 kDa subunit IV; along with four small subunits (3-4 kDa): PetG, PetL, PetM ...

  8. High potential iron–sulfur protein - Wikipedia

    en.wikipedia.org/wiki/High_potential_iron...

    They participate in electron-transfer sequences. The core structure for the [Fe 4 S 4] cluster is a cube with alternating Fe and S vertices. These clusters exist in two oxidation states with a small structural change. Two families of [Fe 4 S 4] clusters are known: the ferredoxin (Fd) family and the high-potential iron–suflur protein (HiPIP ...

  9. SDHB - Wikipedia

    en.wikipedia.org/wiki/SDHB

    The expressed protein weighs 31.6 kDa and is composed of 280 amino acids. [8] [9] SDHB contains the iron-sulphur clusters necessary for tunneling electrons through the complex. It is located between SDHA and the two transmembrane subunits SDHC and SDHD. [10]